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Evaluation of the capacity of gel electrophoresis, steadystate and transient state electrofocusing to resolve native human des‐angiotensin‐I‐angiotensinogen from angiotensinogen
Author(s) -
Auzan Colette,
Genain Claude,
Corvol Pierre,
Menard Joël,
Chrambach Andreas
Publication year - 1985
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150060503
Subject(s) - isoelectric focusing , chromatography , chemistry , polyacrylamide gel electrophoresis , isoelectric point , electrophoresis , gel electrophoresis , angiotensin ii , transient state , biochemistry , enzyme , receptor , electrical engineering , engineering
The resolution of angiotensinogen ( M r 56 800) linked to a decapeptide, angiotensin I ( M r 1295), from the same protein without the decapeptide presents a challenging separation problem. Polyacrylamide gel electrophoresis at an optimized pH of 6.88 is unable to distinguish between the two proteins with statistical significance on the basis of size, but is able to discriminate between them with significance on the basis of their net charge difference. Correspondingly, the proteins are separated in gel electrofocusing with a p I difference of about 0.1 pH unit. For practical purposes, neither the charge separation by gel electrophoresis nor that by steady‐state electrofocusing seems sufficiently convenient. By contrast, transient state electrofocusing provides a ready means for their separation.